Ca 2+ as cofactor of the mitochondrial H + ‐translocating F 1 F O ‐ATP (hydrol)ase
| العنوان: | Ca 2+ as cofactor of the mitochondrial H + ‐translocating |
|---|---|
| المؤلفون: | Alessandra Pagliarani, Salvatore Nesci |
| المصدر: | Proteins: Structure, Function, and Bioinformatics. 89:477-482 |
| بيانات النشر: | Wiley, 2021. |
| سنة النشر: | 2021 |
| مصطلحات موضوعية: | chemistry.chemical_classification, 0303 health sciences, Enzyme complex, Oligomycin, biology, ATP synthase, Chemistry, ATPase, 030302 biochemistry & molecular biology, Mitochondrion, Biochemistry, Cofactor, 03 medical and health sciences, chemistry.chemical_compound, Enzyme, Structural Biology, ATP hydrolysis, biology.protein, Biophysics, Molecular Biology, 030304 developmental biology |
| الوصف: | The mitochondrial F1 FO -ATPase in the presence of the natural cofactor Mg2+ acts as the enzyme of life by synthesizing ATP, but it can also hydrolyze ATP to pump H+ . Interestingly, Mg2+ can be replaced by Ca2+ , but only to sustain ATP hydrolysis and not ATP synthesis. When Ca2+ inserts in F1 , the torque generation built by the chemomechanical coupling between F1 and the rotating central stalk was reported as unable to drive the transmembrane H+ flux within FO . However, the failed H+ translocation is not consistent with the oligomycin-sensitivity of the Ca2+ -dependent F1 FO -ATP(hydrol)ase. New enzyme roles in mitochondrial energy transduction are suggested by recent advances. Accordingly, the structural F1 FO -ATPase distortion driven by ATP hydrolysis sustained by Ca2+ is consistent with the permeability transition pore signal propagation pathway. The Ca2+ -activated F1 FO -ATPase, by forming the pore, may contribute to dissipate the transmembrane H+ gradient created by the same enzyme complex. This article is protected by copyright. All rights reserved. |
| تدمد: | 1097-0134 0887-3585 |
| DOI: | 10.1002/prot.26040 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_________::5bfbd96c07dc91f504c6f0dc9c8988d1 https://doi.org/10.1002/prot.26040 |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi...........5bfbd96c07dc91f504c6f0dc9c8988d1 |
| قاعدة البيانات: | OpenAIRE |
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